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Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F11%3A00360786" target="_blank" >RIV/61388971:_____/11:00360786 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >http://dx.doi.org/10.1016/j.molcatb.2011.03.008</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.molcatb.2011.03.008" target="_blank" >10.1016/j.molcatb.2011.03.008</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Biotransformation of nitriles to hydroxamic acids via a nitrile hydratase?amidase cascade reaction

  • Original language description

    The transformation of benzonitrile into benzohydroxamic acid was performed by a cascade bienzymatic reaction involving nitrile hydration and acyl transfer of the intermediate benzamide onto hydroxylamine. The first step was catalyzed by either a cell-free extract from Rhodococcus erythropolis A4 (nitrile hydratase) or cell-free extracts from recombinant Escherichia coli strains expressing nitrile hydratases from Raoultella terrigena 77.1 and Klebsiella oxytoca 38.1.2; the biocatalyst in the second stepwas a cellfree extract from R. erythropolis A4 (amidase). When using the cell-free extract from R. erythropolis A4 in the first step, the hydrolytic amidase activity was suppressed by ammonium ions, which, however, did not inhibit the acyl transfer reaction catalyzed by the same enzyme. Aromatic and aliphatic nitriles were examined as substrates of the recombinant nitrile hydratases by using a colorimetric assay of hydroxamic acids produced in a coupled acyl transfer reaction

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2011

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Molecular Catalysis B-Enzymatic

  • ISSN

    1381-1177

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    5

  • Pages from-to

    51-55

  • UT code for WoS article

    000291451000008

  • EID of the result in the Scopus database